Purification of bovine serum paraoxonase and its immobilization on Eupergit C 250 L by covalent attachment.


Sayin M., Guler Ö.

Journal of enzyme inhibition and medicinal chemistry, vol.30, no.1, pp.69-74, 2015 (Journal Indexed in SCI Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 30 Issue: 1
  • Publication Date: 2015
  • Doi Number: 10.3109/14756366.2013.879578
  • Title of Journal : Journal of enzyme inhibition and medicinal chemistry
  • Page Numbers: pp.69-74

Abstract

Serum paraoxonase (PON1) is a high-density lipoprotein (HDL)-associated enzyme that protects lipoproteins, both low-density lipoprotein (LDL) and HDL, against oxidation, and is considered as an antioxidative/anti-inflammatory component of HDL. In this study, PON1 was purified from bovine serum by ammonium sulfate precipitation and hydrophobic interaction chromatography on sepharose-4B-L-tyrosine-1-napthylamine. It was then immobilized on an unmodified Eupergit (R) C 250 L support. The immobilized PON1 retained a high catalytic activity and showed increased thermal stability compared to the native enzyme.